Collagen: Collagen triple helix repeat (20 copies)
| PAG Title | Collagen: Collagen triple helix repeat (20 copies) |
| PAG ID | PEX001502 |
| Type | A |
| Source Link |  Pfam |
| Publication Reference | NA |
| PAG Description | Members of this family belong to the collagen superfamily 1. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins 2,3. |
| Species | Homo sapiens |
| Quality Metric Scores | nCoCo Score: 50 |
| Information Content | Rich |
| Other IDs | PF01391 |
| Base PAG ID | PEX001502 |
| Human Phenotyte Annotation | |
| Curator | PAGER curation team |
| Curator Contact | PAGER-contact@googlegroups.com |
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